Skip to main content
Log in

Studies of the expression of subunits α2 and β1 of Na+/K+-ATPase, α1S (L-type) Ca2+-channel, and SERCA 1/2/3 of Ca2+-ATPase of phasic and postural rat muscles in a model of hypogravity using the method of fluorescent microscopy

  • Published:
Cell and Tissue Biology Aims and scope Submit manuscript

Abstract

Using fluorescent microscopy, we found decreased expression of the β1 subunit of Na+/K+-ATPase and subunits of Ca2+-ATPase, increased expression of the α1S subunit of the L-type Ca2+-channel, and no changes in the expression of the α2 subunit of Na+/K+-ATPase in rat postural muscle under the conditions of modeled hypogravity. In the phasic muscle, we observed decreased expression of the β1 subunit, which was similar to that found in the postural muscle, whereas the other studied parameters remained without alterations. However, a decrease in the fluorescence intensity of the β1 subunit was insignificant due to a high variability of data. Thus, hypogravity negatively influenced primarily those skeletal muscles that are responsible for static load.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

m. EDL:

extensor digitorum longus muscle

References

  • Altaeva, E.G., Ogneva, I.V., and Shenkman, B.S., Dynamics of calcium levels and changes SERCA content in muscle fibers of rats and Mongolian gerbils during hind limb unloadings of various duration, Cell Tissue Biol., 2010, vol 4, no. 6, pp. 52, no. 9, pp. 594–599.

    Article  Google Scholar 

  • Blanco, G. and Mercer, R.W., Isozymes of the Na-KATPase: heterogeneity in structure, diversity in function, Am. J. Physiol., 1998, vol. 275, pp. F633–F650.

    CAS  PubMed  Google Scholar 

  • Chow, D.C. and Forte, J.G., Functional significance of the beta-subunit for heterodimeric P-type ATPases, J. Exp. Biol., 1995, vol. 198, pp. 1–17.

    CAS  PubMed  Google Scholar 

  • Eakle, K.A., Kabalm, M.A., Wang, S.G., and Fariey, R.A., The influence of beta subunit structure on the stability of Na+/K(+)-ATPase complexes and interaction with K(+), J. Biol. Chem., 1994, vol. 269, pp. 6550–6557.

    CAS  PubMed  Google Scholar 

  • Genin, A.M., Il’in, A.E., Kaplanskiĭ, A.S., Kasatkina, T.B., Kuznetsova, K.A., Pestov, I.D., and Smirnova, T.A., Bioethics of research on humans and animals in aviation, space and marine medicine, Aviakosm. Ekol. Med., 2001, vol. 35, no. 4, pp. 14–20.

    CAS  Google Scholar 

  • Grigor’ev, A.I., Kozlovskaia, I.B., and Shenkman, B.S., The role of support afferents in organisation of the tonic muscle system, Ross. Fiziol. Zh. Im. I. M. Sechenova, 2004, vol. 90, no. 5, pp. 508, no. 21.

    PubMed  Google Scholar 

  • Kravtsova, V.V., Ogneva, I.V., Altaeva, E.G., Razgovorova, I.A., Tiapkina, O.V., Nikol’skiĭ, E.E., Shenkman, B.S., and Krivoĭ, I.I., Electrogenic activity of Na-KATPase and calcium ions in m. soleus fibers of rats and Mongolian gerbil during simulation of gravitational unloading, Aviakosm. Ekol. Med., 2010, vol. 44, no. 2, pp. 35–44.

    CAS  Google Scholar 

  • Krivoi, I.I., Kravtsova, V.V., Altaeva, E.G., Kubasov, I.V., Prokof'ev, A.V., Drabkina, T.M., Nikol’sky, E.E., and Shenkman, B.S., Decrease in the electrogenic contribution of Na, K-ATPase and resting membrane potential as a possible mechanism of Ca2+ accumulation in rat soleus muscle in a short-term gravity unloading, Biophysics (Moscow), 2008, vol. 53, no. 6, pp. 586–592.

    Article  Google Scholar 

  • Lemas, M.V. and Fanbrough, D.M., Sequence Analysis of DNA Encoding an avian Na+, K(+)-ATPase beta 2-subunit, Biochim. Biophys. Acta, 1993, vol. 1149, pp. 339–342.

    Article  CAS  PubMed  Google Scholar 

  • McDonough, A.A., Geering, K., and Farley, R.A., The sodium pump needs its beta subunit, FASEB J., 2002, vol. 4, pp. 1598–1605.

    Google Scholar 

  • Morey-Holton, E.R. and Globus, R.K., Hindlimb unloading rodent model: technical aspects, J. Appl. Physiol., 2002, vol. 92, pp. 1367–1377.

    Article  PubMed  Google Scholar 

  • Mukhina, A.M., Altaeva, E.G., Nemirovskaia, T.L., and Shenkman, B.S., The role of L-type calcium channels in the accumulation of Ca2+ in soleus muscle fibers in the rat and changes in the ratio of myosin and SERCA isoforms in conditions of gravitational unloading, Ross. Fiziol. Zh. Im. I.M. Sechenova, 2006, vol. 92, no. 11, pp. 1285, no. 1295.

    CAS  PubMed  Google Scholar 

  • Renganathan, M., Wang, Z.M., Messi, M.L., and Delbono, O., Calcium regulates L-type Ca2+ channel expression in rat skeletal muscle cells, Pflugers. Arch., 1999, vol. 438, pp. 649–655.

    CAS  PubMed  Google Scholar 

  • Seok, J.H., Hong, J.H., Jeon, J.R., Hur, G.M., Sung, J.Y., and Lee, J.H., Aldosterone directly induces Na, K-ATPase alpha 1-subunit mRNA in the renal cortex of rat, Biochem. Mol. Biol. Int., 1999, vol. 47, pp. 251–254.

    CAS  PubMed  Google Scholar 

  • Shamraj, O.I. and Lingrel, J.B., A putative fourth Na+, K(+)-ATPase alpha-subunit gene is expressed in testis, Proc. Natl. Acad. Sci. USA., 1994, vol. 91, pp. 12952–12956.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Shao, Y., Ojamaa, K., Klein, I., and Ismail-Beigi, F., Thyroid hormone stimulates Na, K-ATPase gene expression in the hemodynamically unloaded heterotopically transplanted rat heart, Thyroid, 2000, vol. 10, pp. 753–759.

    Article  CAS  PubMed  Google Scholar 

  • Shull, G.E., Greeb, J., and Lingrel, J.B., Molecular cloning of three distinct forms of the Na+, K+-ATPase alpha-subunit from rat brain, Biochemistry, 1986, vol. 25, pp. 8125–8132.

    Article  CAS  PubMed  Google Scholar 

  • Shull, G.E., Schwartz, A., and Lingrel, J.B., Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA, Nature, 1985, vol. 316, pp. 691–695.

    Article  CAS  PubMed  Google Scholar 

  • Skou, J.C. and Esmann, M., The Na, K-ATPase, J. Bioenerg Biomembr., 1992, vol. 24, pp. 249–261.

    CAS  PubMed  Google Scholar 

  • Soukup, T., Zacharová, G., and Smerdu, V., Fibre type composition of soleus and extensor digitorum longus muscles in normal female inbred Lewis rats, Acta Histochem., 2002, vol. 104, pp. 399–405.

    Article  PubMed  Google Scholar 

  • Tyapkina, O., Volkov, E., Nurullin, L., Shenkman, B., Kozlovskaya, I., Nikolsky, E., and Vyskočil, F., Resting membrane potential and Na(+), K(+)-ATPase of rat fast and slow muscles during modeling of hypogravity, Physiol. Res., 2009, vol. 58, pp. 599–603.

    CAS  PubMed  Google Scholar 

  • Tyapkina, O.V., Malomuzh, A.I., Nurullin, L.F., and Nikol’sky, E.E., Quantal and non-quantal acetylcholine release at neuromuscular junctions of muscles of different types in a model of hypogravity, Dokl. Biol. Sci., 2013, vol. 448, pp. 4–6.

    Article  CAS  PubMed  Google Scholar 

  • Tyapkina, O.V., Nurullin, L.F., Petrov, K.A., and Volkov, E.M., The effect of modelling of hypogravity on postsynaptic acetylcholine receptors and activity of acetylcholinesterase in neuromuscular synapses of fast and slow muscles of rat, Cell Tissue Biol., 2014a, vol 8, no. 6, pp. 499–503.

    Google Scholar 

  • Tyapkina, O.V., Volkov, E.M., and Nurullin, L.F., The role of chloride ions in the maintenance of resting membrane potential in rat fast and slow muscles during hypogravity modeling. Bull. Exp. Biol. Med., 2014, vol. 157, no. 5, pp. 577–579.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to E. M. Volkov.

Additional information

Original Russian Text © L.F. Nurullin, O.V. Tyapkina, E.M. Volkov, 2016, published in Tsitologiya, 2016, Vol. 58, No. 6, pp. 444–450.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Nurullin, L.F., Tyapkina, O.V. & Volkov, E.M. Studies of the expression of subunits α2 and β1 of Na+/K+-ATPase, α1S (L-type) Ca2+-channel, and SERCA 1/2/3 of Ca2+-ATPase of phasic and postural rat muscles in a model of hypogravity using the method of fluorescent microscopy. Cell Tiss. Biol. 10, 402–409 (2016). https://doi.org/10.1134/S1990519X16050096

Download citation

  • Received:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1990519X16050096

Keywords

Navigation